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PHD finger protein 1 (Protein PHF1) (hPHF1) (Polycomb-like protein 1) (hPCl1)

 PHF1_HUMAN              Reviewed;         567 AA.
O43189; B1AZX2; B1AZX3; O60929; Q5SU07; Q5SU08; Q96KM7;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
13-FEB-2019, entry version 182.
RecName: Full=PHD finger protein 1;
Short=Protein PHF1;
Short=hPHF1;
AltName: Full=Polycomb-like protein 1;
Short=hPCl1;
Name=PHF1; Synonyms=PCL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-304.
TISSUE=Placenta;
PubMed=9545646; DOI=10.1006/geno.1997.5201;
Coulson M., Robert S., Eyre H.J., Saint R.;
"The identification and localization of a human gene with sequence
similarity to Polycomblike of Drosophila melanogaster.";
Genomics 48:381-383(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT LYS-304.
Wang J.H., Du G.W., Zhou Y., Yuan J.G., Qiang B.Q.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-304.
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-304.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
LYS-304.
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH JAZF1.
PubMed=16397222; DOI=10.1158/0008-5472.CAN-05-2485;
Micci F., Panagopoulos I., Bjerkehagen B., Heim S.;
"Consistent rearrangement of chromosomal band 6p21 with generation of
fusion genes JAZF1/PHF1 and EPC1/PHF1 in endometrial stromal
sarcoma.";
Cancer Res. 66:107-112(2006).
[7]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
THE PRC2 COMPLEX.
PubMed=18086877; DOI=10.1128/MCB.01589-07;
Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.;
"Role of hPHF1 in H3K27 methylation and Hox gene silencing.";
Mol. Cell. Biol. 28:1862-1872(2008).
[8]
FUNCTION, INTERACTION WITH THE PRC2 COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=18285464; DOI=10.1128/MCB.02017-07;
Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.;
"Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27
trimethylation in vivo.";
Mol. Cell. Biol. 28:2718-2731(2008).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18385154; DOI=10.1093/nar/gkn146;
Hong Z., Jiang J., Lan L., Nakajima S., Kanno S., Koseki H., Yasui A.;
"A polycomb group protein, PHF1, is involved in the response to DNA
double-strand breaks in human cell.";
Nucleic Acids Res. 36:2939-2947(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 (ISOFORM 1), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
SUBCELLULAR LOCATION.
PubMed=20873783; DOI=10.1021/pr100562w;
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C.,
Santana Bernachi J., Paes Leme A.F., Kobarg J.;
"Characterization of hNek6 interactome reveals an important role for
its short N-terminal domain and colocalization with proteins at the
centrosome.";
J. Proteome Res. 9:6298-6316(2010).
[12]
DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH MEAF6.
PubMed=22761769; DOI=10.1371/journal.pone.0039354;
Panagopoulos I., Micci F., Thorsen J., Gorunova L., Eibak A.M.,
Bjerkehagen B., Davidson B., Heim S.;
"Novel fusion of MYST/Esa1-associated factor 6 and PHF1 in endometrial
stromal sarcoma.";
PLoS ONE 7:E39354-E39354(2012).
[13]
H3K36ME3-BINDING.
PubMed=23228662; DOI=10.1016/j.bbrc.2012.11.116;
Qin S., Guo Y., Xu C., Bian C., Fu M., Gong S., Min J.;
"Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind
to histone H3K36me3.";
Biochem. Biophys. Res. Commun. 430:547-553(2013).
[14]
FUNCTION, INTERACTION WITH TP53, AND SUBCELLULAR LOCATION.
PubMed=23150668; DOI=10.1074/jbc.M111.338996;
Yang Y., Wang C., Zhang P., Gao K., Wang D., Yu H., Zhang T.,
Jiang S., Hexige S., Hong Z., Yasui A., Liu J.O., Huang H., Yu L.;
"Polycomb group protein PHF1 regulates p53-dependent cell growth
arrest and apoptosis.";
J. Biol. Chem. 288:529-539(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
STRUCTURE BY NMR OF 29-85.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the Tudor domain of PHD finger protein 1 (PHF1
protein).";
Submitted (JUN-2007) to the PDB data bank.
[18]
STRUCTURE BY NMR OF 6-83, FUNCTION, H3K36ME3-BINDING, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF TRP-41; TYR-47; PHE-65; GLU-66 AND
PHE-71.
PubMed=23273982; DOI=10.1016/j.molcel.2012.11.026;
Cai L., Rothbart S.B., Lu R., Xu B., Chen W.Y., Tripathy A.,
Rockowitz S., Zheng D., Patel D.J., Allis C.D., Strahl B.D., Song J.,
Wang G.G.;
"An H3K36 methylation-engaging Tudor motif of Polycomb-like proteins
mediates PRC2 complex targeting.";
Mol. Cell 49:571-582(2013).
[19]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 28-85, FUNCTION,
H3K36ME3-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-41 AND
TYR-47.
PubMed=23142980; DOI=10.1038/nsmb.2435;
Musselman C.A., Avvakumov N., Watanabe R., Abraham C.G., Lalonde M.E.,
Hong Z., Allen C., Roy S., Nunez J.K., Nickoloff J., Kulesza C.A.,
Yasui A., Cote J., Kutateladze T.G.;
"Molecular basis for H3K36me3 recognition by the Tudor domain of
PHF1.";
Nat. Struct. Mol. Biol. 19:1266-1272(2012).
-!- FUNCTION: Polycomb group (PcG) that specifically binds histone H3
trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2
complex. Involved in DNA damage response and is recruited at
double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark
for transcriptional activation, and recruiting the PRC2 complex:
it is however unclear whether recruitment of the PRC2 complex to
H3K36me3 leads to enhance or inhibit H3K27me3 methylation mediated
by the PRC2 complex. According to some reports, PRC2 recruitment
by PHF1 promotes H3K27me3 and subsequent gene silencing by
inducing spreading of PRC2 and H3K27me3 into H3K36me3 loci
(PubMed:18285464 and PubMed:23273982). According to another
report, PHF1 recruits the PRC2 complex at double-strand breaks
(DSBs) and inhibits the activity of PRC2 (PubMed:23142980).
Regulates p53/TP53 stability and prolonges its turnover: may act
by specifically binding to a methylated from of p53/TP53.
{ECO:0000269|PubMed:18086877, ECO:0000269|PubMed:18285464,
ECO:0000269|PubMed:18385154, ECO:0000269|PubMed:23142980,
ECO:0000269|PubMed:23150668, ECO:0000269|PubMed:23273982}.
-!- SUBUNIT: Interacts with CHMP1 (By similarity). Associated
component of the PRC2 complex. Interacts with p53/TP53.
{ECO:0000250, ECO:0000269|PubMed:18086877,
ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:23150668}.
-!- INTERACTION:
Q9ULK2:ATXN7L1; NbExp=3; IntAct=EBI-530034, EBI-310660;
Q96CA5:BIRC7; NbExp=3; IntAct=EBI-530034, EBI-517623;
Q13137:CALCOCO2; NbExp=3; IntAct=EBI-530034, EBI-739580;
Q15910:EZH2; NbExp=5; IntAct=EBI-530034, EBI-530054;
Q9BPX1:HSD17B14; NbExp=5; IntAct=EBI-530034, EBI-742664;
Q15742:NAB2; NbExp=5; IntAct=EBI-530034, EBI-8641936;
Q9NR12:PDLIM7; NbExp=3; IntAct=EBI-530034, EBI-350517;
Q93062:RBPMS; NbExp=4; IntAct=EBI-530034, EBI-740322;
Q12800:TFCP2; NbExp=4; IntAct=EBI-530034, EBI-717422;
Q9NVV9:THAP1; NbExp=3; IntAct=EBI-530034, EBI-741515;
P36406:TRIM23; NbExp=3; IntAct=EBI-530034, EBI-740098;
Q08AM6:VAC14; NbExp=3; IntAct=EBI-530034, EBI-2107455;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Note=Localizes
specifically to the promoters of numerous target genes. Localizes
to double-strand breaks (DSBs) sites following DNA damage. Co-
localizes with NEK6 in the centrosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2; Synonyms=PHF2;
IsoId=O43189-1; Sequence=Displayed;
Name=1; Synonyms=PHF1;
IsoId=O43189-2; Sequence=VSP_004694, VSP_004695;
Note=Contains a phosphoserine at position 360.
{ECO:0000244|PubMed:18669648};
-!- TISSUE SPECIFICITY: Highest levels in heart, skeletal muscle, and
pancreas, lower levels in brain, placenta, lung, liver and kidney.
-!- DOMAIN: The Tudor domain recognizes and binds H3K36me3
(PubMed:23228662, PubMed:23273982 and PubMed:23142980).
-!- DISEASE: Note=A chromosomal aberration involving PHF1 may be a
cause of endometrial stromal tumors. Translocation t(6;7)(p21;p22)
with JAZF1. Translocation t(1;6)(p34;p21) with MEAF6.
{ECO:0000269|PubMed:16397222, ECO:0000269|PubMed:22761769}.
-!- SIMILARITY: Belongs to the Polycomblike family. {ECO:0000305}.
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EMBL; AF029678; AAC52062.1; -; mRNA.
EMBL; AF052205; AAC13273.1; -; mRNA.
EMBL; AL662799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL021366; CAA16158.1; -; Genomic_DNA.
EMBL; AL021366; CAA16159.1; -; Genomic_DNA.
EMBL; AL050332; CAC38366.1; -; Genomic_DNA.
EMBL; AL050332; CAC38367.1; -; Genomic_DNA.
EMBL; BX088650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03729.1; -; Genomic_DNA.
EMBL; CH471081; EAX03730.1; -; Genomic_DNA.
EMBL; BC008834; AAH08834.1; -; mRNA.
CCDS; CCDS4777.1; -. [O43189-1]
CCDS; CCDS4778.1; -. [O43189-2]
RefSeq; NP_002627.1; NM_002636.4.
RefSeq; NP_077084.1; NM_024165.2.
RefSeq; XP_011512964.1; XM_011514662.1. [O43189-1]
UniGene; Hs.166204; -.
PDB; 2E5P; NMR; -; A=29-83.
PDB; 2M0O; NMR; -; A=6-83.
PDB; 4HCZ; X-ray; 1.85 A; A/B=28-85.
PDB; 5XFN; X-ray; 1.90 A; A=25-340.
PDB; 5XFO; X-ray; 1.90 A; A=25-340.
PDB; 5XFP; X-ray; 2.30 A; A/B/E=25-360.
PDBsum; 2E5P; -.
PDBsum; 2M0O; -.
PDBsum; 4HCZ; -.
PDBsum; 5XFN; -.
PDBsum; 5XFO; -.
PDBsum; 5XFP; -.
ProteinModelPortal; O43189; -.
SMR; O43189; -.
BioGrid; 111271; 63.
DIP; DIP-34001N; -.
IntAct; O43189; 80.
MINT; O43189; -.
STRING; 9606.ENSP00000363640; -.
BindingDB; O43189; -.
iPTMnet; O43189; -.
PhosphoSitePlus; O43189; -.
BioMuta; PHF1; -.
EPD; O43189; -.
jPOST; O43189; -.
MaxQB; O43189; -.
PaxDb; O43189; -.
PeptideAtlas; O43189; -.
PRIDE; O43189; -.
ProteomicsDB; 48805; -.
ProteomicsDB; 48806; -. [O43189-2]
DNASU; 5252; -.
Ensembl; ENST00000374512; ENSP00000363636; ENSG00000112511. [O43189-2]
Ensembl; ENST00000374516; ENSP00000363640; ENSG00000112511. [O43189-1]
Ensembl; ENST00000427869; ENSP00000391901; ENSG00000225553.
Ensembl; ENST00000454914; ENSP00000407295; ENSG00000225553.
GeneID; 5252; -.
KEGG; hsa:5252; -.
UCSC; uc003oeh.4; human. [O43189-1]
CTD; 5252; -.
DisGeNET; 5252; -.
EuPathDB; HostDB:ENSG00000112511.17; -.
GeneCards; PHF1; -.
HGNC; HGNC:8919; PHF1.
HPA; HPA031038; -.
MIM; 602881; gene.
neXtProt; NX_O43189; -.
OpenTargets; ENSG00000112511; -.
PharmGKB; PA33259; -.
eggNOG; KOG4323; Eukaryota.
eggNOG; ENOG410XQ6E; LUCA.
GeneTree; ENSGT00390000009222; -.
HOVERGEN; HBG004755; -.
InParanoid; O43189; -.
KO; K11467; -.
OMA; APPLWDP; -.
OrthoDB; 281828at2759; -.
PhylomeDB; O43189; -.
TreeFam; TF106420; -.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
ChiTaRS; PHF1; human.
EvolutionaryTrace; O43189; -.
GeneWiki; PHF1; -.
GenomeRNAi; 5252; -.
PRO; PR:O43189; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112511; Expressed in 232 organ(s), highest expression level in left testis.
ExpressionAtlas; O43189; baseline and differential.
Genevisible; O43189; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:UniProtKB.
GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR040477; KDM4_Tudor_2.
InterPro; IPR025894; Mtf2_C_dom.
InterPro; IPR031202; PHF1.
InterPro; IPR002999; Tudor.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR12628:SF11; PTHR12628:SF11; 1.
Pfam; PF14061; Mtf2_C; 1.
Pfam; PF00628; PHD; 1.
Pfam; PF18104; Tudor_2; 1.
SMART; SM00249; PHD; 2.
SMART; SM00333; TUDOR; 1.
SUPFAM; SSF57903; SSF57903; 2.
PROSITE; PS01359; ZF_PHD_1; 2.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Chromosomal rearrangement; Complete proteome; Cytoplasm; Cytoskeleton;
DNA damage; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 567 PHD finger protein 1.
/FTId=PRO_0000059288.
DOMAIN 29 86 Tudor.
ZN_FING 87 142 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 186 240 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 350 457 SFPSGQGPGGGVSRPLGKRRRPEPEPLRRRQKGKVEELGPP
SAVRNQPEPQEQRERAHLQRALQASVSPPSPSPNQSYQGSS
GYNFRPTDARCLPSSPIRMFASFHPS -> RAGPWGRGLTS
PGEAPEAGARAPEEEAEGESGGAGATLSSAQSARAPGAEGA
GSSAEGTAAAPSGCLLPSTLLPAPQGPLGTVDPQTGHPWNF
TLVSPQTSLKVPPTR (in isoform 1).
{ECO:0000303|PubMed:9545646}.
/FTId=VSP_004694.
VAR_SEQ 458 567 Missing (in isoform 1).
{ECO:0000303|PubMed:9545646}.
/FTId=VSP_004695.
VARIANT 42 42 T -> S (in dbSNP:rs6934613).
/FTId=VAR_044500.
VARIANT 304 304 R -> K (in dbSNP:rs3116713).
{ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9545646,
ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
/FTId=VAR_034382.
MUTAGEN 41 41 W->A: Abolishes histone H3K36me3-binding
and localization at double-strand breaks
(DSBs). {ECO:0000269|PubMed:23142980,
ECO:0000269|PubMed:23273982}.
MUTAGEN 47 47 Y->A: Abolishes histone H3K36me3-binding.
{ECO:0000269|PubMed:23142980,
ECO:0000269|PubMed:23273982}.
MUTAGEN 65 65 F->A: Abolishes histone H3K36me3-binding.
{ECO:0000269|PubMed:23273982}.
MUTAGEN 66 66 E->K: Impairs histone H3K36me3-binding.
{ECO:0000269|PubMed:23273982}.
MUTAGEN 71 71 F->A: Abolishes histone H3K36me3-binding.
{ECO:0000269|PubMed:23273982}.
STRAND 36 40 {ECO:0000244|PDB:4HCZ}.
STRAND 46 55 {ECO:0000244|PDB:4HCZ}.
TURN 56 59 {ECO:0000244|PDB:4HCZ}.
STRAND 60 65 {ECO:0000244|PDB:4HCZ}.
TURN 66 68 {ECO:0000244|PDB:2E5P}.
STRAND 70 74 {ECO:0000244|PDB:4HCZ}.
HELIX 75 77 {ECO:0000244|PDB:4HCZ}.
STRAND 78 80 {ECO:0000244|PDB:4HCZ}.
STRAND 87 90 {ECO:0000244|PDB:5XFO}.
TURN 91 93 {ECO:0000244|PDB:5XFN}.
STRAND 104 106 {ECO:0000244|PDB:5XFN}.
TURN 108 110 {ECO:0000244|PDB:5XFN}.
STRAND 113 115 {ECO:0000244|PDB:5XFN}.
HELIX 116 118 {ECO:0000244|PDB:5XFN}.
STRAND 119 121 {ECO:0000244|PDB:5XFN}.
STRAND 129 133 {ECO:0000244|PDB:5XFO}.
HELIX 137 144 {ECO:0000244|PDB:5XFN}.
HELIX 155 163 {ECO:0000244|PDB:5XFN}.
HELIX 171 173 {ECO:0000244|PDB:5XFO}.
TURN 189 191 {ECO:0000244|PDB:5XFN}.
TURN 197 200 {ECO:0000244|PDB:5XFN}.
STRAND 201 203 {ECO:0000244|PDB:5XFN}.
TURN 205 207 {ECO:0000244|PDB:5XFN}.
STRAND 210 212 {ECO:0000244|PDB:5XFN}.
HELIX 213 215 {ECO:0000244|PDB:5XFN}.
STRAND 230 233 {ECO:0000244|PDB:5XFN}.
HELIX 235 238 {ECO:0000244|PDB:5XFN}.
STRAND 243 246 {ECO:0000244|PDB:5XFN}.
HELIX 251 266 {ECO:0000244|PDB:5XFN}.
TURN 273 276 {ECO:0000244|PDB:5XFN}.
HELIX 277 283 {ECO:0000244|PDB:5XFN}.
HELIX 285 288 {ECO:0000244|PDB:5XFN}.
HELIX 291 295 {ECO:0000244|PDB:5XFN}.
TURN 298 300 {ECO:0000244|PDB:5XFN}.
HELIX 301 311 {ECO:0000244|PDB:5XFN}.
TURN 313 315 {ECO:0000244|PDB:5XFN}.
STRAND 316 318 {ECO:0000244|PDB:5XFN}.
HELIX 322 324 {ECO:0000244|PDB:5XFO}.
STRAND 328 332 {ECO:0000244|PDB:5XFN}.
SEQUENCE 567 AA; 62106 MW; E81BA9475565957C CRC64;
MAQPPRLSRS GASSLWDPAS PAPTSGPRPR LWEGQDVLAR WTDGLLYLGT IKKVDSAREV
CLVQFEDDSQ FLVLWKDISP AALPGEELLC CVCRSETVVP GNRLVSCEKC RHAYHQDCHV
PRAPAPGEGE GTSWVCRQCV FAIATKRGGA LKKGPYARAM LGMKLSLPYG LKGLDWDAGH
LSNRQQSYCY CGGPGEWNLK MLQCRSCLQW FHEACTQCLS KPLLYGDRFY EFECCVCRGG
PEKVRRLQLR WVDVAHLVLY HLSVCCKKKY FDFDREILPF TSENWDSLLL GELSDTPKGE
RSSRLLSALN SHKDRFISGR EIKKRKCLFG LHARMPPPVE PPTGDGALTS FPSGQGPGGG
VSRPLGKRRR PEPEPLRRRQ KGKVEELGPP SAVRNQPEPQ EQRERAHLQR ALQASVSPPS
PSPNQSYQGS SGYNFRPTDA RCLPSSPIRM FASFHPSAST AGTSGDSGPP DRSPLELHIG
FPTDIPKSAP HSMTASSSSV SSPSPGLPRR SAPPSPLCRS LSPGTGGGVR GGVGYLSRGD
PVRVLARRVR PDGSVQYLVE WGGGGIF


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Pathways :
WP2199: Seed Development
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining

Related Genes :
[PHF1 PCL1] PHD finger protein 1 (Protein PHF1) (hPHF1) (Polycomb-like protein 1) (hPCl1)
[Phf1 Plc1 Tctex-3 Tctex3] PHD finger protein 1 (Protein PHF1) (Polycomb-like protein 1) (mPCl1) (T-complex testis-expressed 3)
[SUZ12 CHET9 JJAZ1 KIAA0160] Polycomb protein SUZ12 (Chromatin precipitated E2F target 9 protein) (ChET 9 protein) (Joined to JAZF1 protein) (Suppressor of zeste 12 protein homolog)
[EED] Polycomb protein EED (hEED) (Embryonic ectoderm development protein) (WD protein associating with integrin cytoplasmic tails 1) (WAIT-1)
[phf1 saf50 swp1 SPCC4G3.07c] SWM histone demethylase complex subunit phf1 (PHD finger domain-containing protein phf1)
[EZH2 KMT6] Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.43) (ENX-1) (Enhancer of zeste homolog 2) (Lysine N-methyltransferase 6)
[Ezh2 Enx1h] Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.43) (ENX-1) (Enhancer of zeste homolog 2)
[PHF19 PCL3] PHD finger protein 19 (Polycomb-like protein 3) (hPCL3)
[HPCAL1 BDR1] Hippocalcin-like protein 1 (Calcium-binding protein BDR-1) (HLP2) (Visinin-like protein 3) (VILIP-3)
[MEAF6 C1orf149 CENP-28 EAF6] Chromatin modification-related protein MEAF6 (MYST/Esa1-associated factor 6) (Esa1-associated factor 6 homolog) (Protein EAF6 homolog) (hEAF6) (Sarcoma antigen NY-SAR-91)
[Chmp1a Chmp1 Pcoln3] Charged multivesicular body protein 1a (Chromatin-modifying protein 1a) (CHMP1a)
[BIRC7 KIAP LIVIN MLIAP RNF50 UNQ5800/PRO19607/PRO21344] Baculoviral IAP repeat-containing protein 7 (EC 2.3.2.27) (Kidney inhibitor of apoptosis protein) (KIAP) (Livin) (Melanoma inhibitor of apoptosis protein) (ML-IAP) (RING finger protein 50) (RING-type E3 ubiquitin transferase BIRC7) [Cleaved into: Baculoviral IAP repeat-containing protein 7 30kDa subunit (Truncated livin) (p30-Livin) (tLivin)]
[CHMP1A CHMP1 KIAA0047 PCOLN3 PRSM1] Charged multivesicular body protein 1a (Chromatin-modifying protein 1a) (CHMP1a) (Vacuolar protein sorting-associated protein 46-1) (Vps46-1) (hVps46-1)
[Phf19 Pcl3] PHD finger protein 19 (Polycomb-like protein 3)
[JADE1 KIAA1807 PHF17] Protein Jade-1 (Jade family PHD finger protein 1) (PHD finger protein 17)
[Jade1 Kiaa1807 Phf17] Protein Jade-1 (Jade family PHD finger protein 1) (PHD finger protein 17)
[Uhrf1 Np95] E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) (Nuclear protein 95) (Nuclear zinc finger protein Np95) (RING-type E3 ubiquitin transferase UHRF1) (Ubiquitin-like PHD and RING finger domain-containing protein 1) (mUhrf1) (Ubiquitin-like-containing PHD and RING finger domains protein 1)
[THAP1] THAP domain-containing protein 1
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[RING1A RF434 At5g44280 K9L2.3] Putative E3 ubiquitin-protein ligase RING1a (EC 2.3.2.27) (Polycomb complex protein RING1a) (Protein RING1a) (AtRING1a) (RING-type E3 ubiquitin transferase RING1a) (Ring finger protein 434)
[Jade2 Kiaa0239 Phf15] E3 ubiquitin-protein ligase Jade-2 (EC 2.3.2.27) (Jade family PHD finger protein 2) (PHD finger protein 15)
[JADE2 KIAA0239 PHF15] E3 ubiquitin-protein ligase Jade-2 (EC 2.3.2.27) (Jade family PHD finger protein 2) (PHD finger protein 15)
[Pcgf2 Mel-18 Mel18 Rnf110 Zfp144 Znf144] Polycomb group RING finger protein 2 (DNA-binding protein Mel-18) (Melanoma nuclear protein 18) (RING finger protein 110) (Zinc finger protein 144) (Zfp-144)
[RNF2 BAP1 DING HIPI3 RING1B] E3 ubiquitin-protein ligase RING2 (EC 2.3.2.27) (Huntingtin-interacting protein 2-interacting protein 3) (HIP2-interacting protein 3) (Protein DinG) (RING finger protein 1B) (RING1b) (RING finger protein 2) (RING finger protein BAP-1) (RING-type E3 ubiquitin transferase RING2)
[NEK6] Serine/threonine-protein kinase Nek6 (EC 2.7.11.1) (Never in mitosis A-related kinase 6) (NimA-related protein kinase 6) (Protein kinase SID6-1512)
[BMI1 BMI-1 PCGF4] Polycomb complex protein BMI-1 (Polycomb group RING finger protein 4)
[Nek6] Serine/threonine-protein kinase Nek6 (EC 2.7.11.1) (Never in mitosis A-related kinase 6) (NimA-related protein kinase 6)
[Nek6] Serine/threonine-protein kinase Nek6 (EC 2.7.11.1) (Never in mitosis A-related kinase 6) (NimA-related protein kinase 6)
[CXXC1 CFP1 CGBP PCCX1 PHF18] CXXC-type zinc finger protein 1 (CpG-binding protein) (PHD finger and CXXC domain-containing protein 1)
[PCGF2 MEL18 RNF110 ZNF144] Polycomb group RING finger protein 2 (DNA-binding protein Mel-18) (RING finger protein 110) (Zinc finger protein 144)

Bibliography :
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